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• W2996060168 abstract "The FANCJ helicase unfolds G-quadruplexes (G4s) in human cells to support DNA replication. This action is coupled to the recruitment of REV1 polymerase to synthesize DNA across from a guanine template. The precise mechanisms of these reactions remain unclear. While FANCJ binds to G4s with an AKKQ motif, it is not known whether this site recognizes damaged G4 structures. FANCJ also has a PIP-like (PCNA Interacting Protein) region that may recruit REV1 to G4s either directly or through interactions mediated by PCNA protein. In this work, we measured the affinities of a FANCJ AKKQ peptide for G4s formed by (TTAGGG)4 and (GGGT)4 using fluorescence spectroscopy and biolayer interferometry (BLI). The effects of 8-oxoguanine (8oxoG) on these interactions were tested at different positions. BLI assays were then performed with a FANCJ PIP to examine its recruitment of REV1 and PCNA. FANCJ AKKQ bound tightly to a TTA loop and was sequestered away from the 8oxoG. Reducing the loop length between guanine tetrads increased the affinity of the peptide for 8oxoG4s. FANCJ PIP targeted both REV1 and PCNA but favored interactions with the REV1 polymerase. The impact of these results on the remodeling of damaged G4 DNA is discussed herein." @default.
• W2996060168 created "2019-12-26" @default.
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• W2996060168 creator A5074437248 @default.
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• W2996060168 date "2019-12-19" @default.
• W2996060168 modified "2023-09-29" @default.
• W2996060168 title "Assembly of a G-Quadruplex Repair Complex by the FANCJ DNA Helicase and the REV1 Polymerase" @default.
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• W2996060168 doi "https://doi.org/10.3390/genes11010005" @default.
• W2996060168 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7017153" @default.
• W2996060168 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/31861576" @default.
• W2996060168 hasPublicationYear "2019" @default.
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